Research workbench

hMiro1 EF hand and cGTPase domains in the GDP-bound state

Analyse hMiro1 EF hand and cGTPase domains in the GDP-bound state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5KU1
Type: protein
Length: 398 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.501
Source: Homo sapiens
Molecule: Mitochondrial Rho GTPase 1
EC: 3.6.5.-
UniProt: Q8IXI2
Ligands: GDP, MG, CL
Pockets: 10 · best druggability 0.63

Structure

x-ray diffraction · resolution 2.501 · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitochondrial Rho GTPase 1 (EC 3.6.5.-)	protein	398	44% helix, 15% strand	Q8IXI2

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
CL · Chloride ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	134	0.63	0.85	19	empty
2	209	0.51	0.76	32	GDP, CL
3	60	0.49	0.85	14	empty
4	154	0.48	0.77	29	empty
5	53	0.41	0.81	15	empty

Compared structures

5KU1 · HMIRO1 ef hand and cgtpase domains in the GDP-bound state · the same entry in another collection · chain A against A, TM-score 1.00
Q8IXI2 · AlphaFold monomer V2.0 prediction for mitochondrial rho GTPase 1 (Q8IXI2) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8IXI2
Elsewhere: RCSB PDB 5KU1 · PDBe 5KU1 · UniProt Q8IXI2

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